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A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria

Author

Listed:
  • Stephanie K. Aoki

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Elie J. Diner

    (Biomolecular Science and Engineering Program, University of California – Santa Barbara (UCSB))

  • Claire t’Kint de Roodenbeke

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Brandt R. Burgess

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Stephen J. Poole

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Bruce A. Braaten

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Allison M. Jones

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Julia S. Webb

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB))

  • Christopher S. Hayes

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
    Biomolecular Science and Engineering Program, University of California – Santa Barbara (UCSB))

  • Peggy A. Cotter

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
    Biomolecular Science and Engineering Program, University of California – Santa Barbara (UCSB)
    Present address: Department of Microbiology and Immunology, School of Medicine, University of North Carolina – Chapel Hill, Chapel Hill, North Carolina 27599-7290, USA.)

  • David A. Low

    (Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
    Biomolecular Science and Engineering Program, University of California – Santa Barbara (UCSB))

Abstract

Contact toxins in bacteria Contact-dependent growth inhibition (CDI), first described in Escherichia coli five years ago, is a mechanism by which cell-to-cell contact inhibits the growth of bacterial cells that do not have this system. CDI is mediated by the two-partner secretion proteins CdiA and CdiB, and a small immunity protein CdiI gives protection against autoinhibition. The molecular basis for some of the interactions involved in CDI has now been elucidated; the toxic properties of CdiA are contained within the protein's carboxy-terminal end (CdiA-CT). A search across other E. coli strains and bacterial species shows the system to be widespread — a range of bacteria contain one or more CdiA homologues, with varied CdiA-CT toxin sequences. These findings suggest that CDI systems constitute an intricate immunity network with an important function in bacterial growth competition in the environment.

Suggested Citation

  • Stephanie K. Aoki & Elie J. Diner & Claire t’Kint de Roodenbeke & Brandt R. Burgess & Stephen J. Poole & Bruce A. Braaten & Allison M. Jones & Julia S. Webb & Christopher S. Hayes & Peggy A. Cotter & , 2010. "A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria," Nature, Nature, vol. 468(7322), pages 439-442, November.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7322:d:10.1038_nature09490
    DOI: 10.1038/nature09490
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    Cited by:

    1. William P J Smith & Andrea Vettiger & Julius Winter & Till Ryser & Laurie E Comstock & Marek Basler & Kevin R Foster, 2020. "The evolution of the type VI secretion system as a disintegration weapon," PLOS Biology, Public Library of Science, vol. 18(5), pages 1-26, May.
    2. Nicholas L. Bartelli & Victor J. Passanisi & Karolina Michalska & Kiho Song & Dinh Q. Nhan & Hongjun Zhou & Bonnie J. Cuthbert & Lucy M. Stols & William H. Eschenfeldt & Nicholas G. Wilson & Jesse S. , 2022. "Proteolytic processing induces a conformational switch required for antibacterial toxin delivery," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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